1ivt

NMR structures of the C-terminal globular domain of human lamin A/C

Method: SOLUTION NMR Dmax: 53.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Lamin A/C

Homo sapiens

UniProt P02545

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 428–549 Fragment:C-terminal domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.3;303 K;Pressure ambient NMR sample composition:1mM U-15N,13C; 20mM phosphate buffer K | 90% H2O/10% D2O NMR sample composition:1mM U-15N; 20mM phosphate buffer K | 90% H2O/10% D2O NMR sample composition:1mM U-15N,13C; 20mM phosphate buffer K | 100% D2O Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

24 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LAMA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–122; UniProt 428–549

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1ivt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ivt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ivt
Deposition date deposition_date2002-03-29
Structure title titleNMR structures of the C-terminal globular domain of human lamin A/C
Keywords keywordsBeta barrel, ALL SHEET, Ig-fold, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.35
Radius of gyration Rg (electron density) rg_electron13.98
Forward intensity I(0) i0617673000.00
Molecular weight molecular_weight202130.0 kDa
Excluded volume excluded_volume250020 ų
Envelope volume envelope_volume28506 ų
Hydration-shell volume shell_volume15141 ų
Envelope diameter envelope_diameter59.9
Shell Rg shell_rg22.00
Envelope Rg envelope_rg16.44
Shape Rg shape_rg13.95
Total Rg total_rg14.26
Total atoms total_atoms28290
Residues n_residues1830
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax53.7
Rg (real space) rg_real14.30
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real6.1770e+08
I(0) uncertainty (real space) i0_real_error7.6690e+06
Rg (reciprocal space) rg_reciprocal14.30
I(0) (reciprocal space) i0_reciprocal617700000.0000
Solution quality estimate total_estimate0.8249
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.311
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha384700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.598; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ivta_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.16 — Lamin A/C globular tail domain
Family Family familyb.1.16.1 — Lamin A/C globular tail domain

CATH v4.4 (1 domains)

Domain ID domain_id1ivtA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1260 — Lamin Tail domain

8. Citations (1)

9. Files and Curves (10)